User:James Bahng/sandbox 1
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
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| + | FAH is a homodimer made up of two 46 kDa subunits. The subunits form a cavity complementary in shape and charge to fumarylacetoacetate. The binding is coordinated by Ca2+, Arg and two Tyr. The active residues in are His-133, acting as a base to activate a water, and Arg-237, Gln-240 and Lys-253 acting to stablize the tetrahedral alkoxy transition state. | ||
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | ||
Revision as of 15:38, 31 March 2014
Structure of Fumarylacetoacetate Hydrolase with Phosphorus-based Inhibitor
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
